You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000002474_02578
You are here: Home > Sequence: MGYG000002474_02578
Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Rahnella variigena | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Rahnella; Rahnella variigena | |||||||||||
| CAZyme ID | MGYG000002474_02578 | |||||||||||
| CAZy Family | PL1 | |||||||||||
| CAZyme Description | Pectate lyase A | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 20227; End: 21324 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| PL1 | 78 | 286 | 1.7e-76 | 0.9859154929577465 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam00544 | Pec_lyase_C | 3.10e-64 | 57 | 286 | 1 | 211 | Pectate lyase. This enzyme forms a right handed beta helix structure. Pectate lyase is an enzyme involved in the maceration and soft rotting of plant tissue. |
| smart00656 | Amb_all | 1.96e-52 | 81 | 286 | 7 | 186 | Amb_all domain. |
| COG3866 | PelB | 2.91e-52 | 17 | 356 | 34 | 340 | Pectate lyase [Carbohydrate transport and metabolism]. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| CAD7205097.1 | 4.41e-260 | 19 | 365 | 125 | 471 |
| QNK08233.1 | 3.31e-204 | 1 | 365 | 1 | 375 |
| QAX78175.1 | 3.94e-154 | 19 | 364 | 22 | 367 |
| AYH49086.1 | 1.87e-120 | 19 | 356 | 52 | 396 |
| QOH53179.1 | 3.76e-120 | 19 | 356 | 52 | 396 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1OOC_A | 3.21e-113 | 19 | 357 | 16 | 358 | ChainA, Pectate lyase A [Dickeya chrysanthemi],1OOC_B Chain B, Pectate lyase A [Dickeya chrysanthemi],1PE9_A Chain A, Pectate lyase A [Dickeya chrysanthemi],1PE9_B Chain B, Pectate lyase A [Dickeya chrysanthemi] |
| 1JRG_A | 1.29e-112 | 19 | 357 | 16 | 358 | ChainA, Pectate lyase [Dickeya chrysanthemi],1JRG_B Chain B, Pectate lyase [Dickeya chrysanthemi],1JTA_A Chain A, pectate lyase A [Dickeya chrysanthemi] |
| 1PCL_A | 2.26e-109 | 19 | 356 | 10 | 351 | ChainA, PECTATE LYASE E [Dickeya chrysanthemi] |
| 1VBL_A | 5.43e-54 | 19 | 287 | 13 | 331 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
| 5AMV_A | 1.60e-51 | 19 | 334 | 13 | 373 | Structuralinsights into the loss of catalytic competence in pectate lyase at low pH [Bacillus subtilis],5X2I_A Polygalacturonate Lyase by Fusing with a Self-assembling Amphipathic Peptide [Bacillus subtilis subsp. subtilis str. 168] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P0C1A4 | 5.60e-119 | 19 | 356 | 56 | 400 | Pectate lyase E OS=Dickeya chrysanthemi OX=556 GN=pelE PE=3 SV=1 |
| P0C1A5 | 2.25e-118 | 19 | 356 | 56 | 400 | Pectate lyase E OS=Dickeya dadantii (strain 3937) OX=198628 GN=pelE PE=3 SV=2 |
| P0C1A3 | 1.84e-114 | 18 | 357 | 46 | 389 | Pectate lyase A OS=Dickeya dadantii (strain 3937) OX=198628 GN=pelA PE=1 SV=1 |
| P0C1A2 | 2.01e-111 | 19 | 357 | 48 | 390 | Pectate lyase A OS=Dickeya chrysanthemi OX=556 GN=pelA PE=1 SV=1 |
| P18209 | 1.97e-108 | 19 | 356 | 45 | 387 | Pectate lyase D OS=Dickeya chrysanthemi OX=556 GN=pelD PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000052 | 0.000012 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |